Rapid Profiling of the Glycosylation Effects on the Binding of SARS-CoV-2 Spike Protein to Angiotensin-Converting Enzyme 2 Using MALDI-MS with High Mass Detection-Reference-Cited by-同舟云学术

Rapid Profiling of the Glycosylation Effects on the Binding of SARS-CoV-2 Spike Protein to Angiotensin-Converting Enzyme 2 Using MALDI-MS with High Mass Detection

Published:2024-01-27 Issue:5 Volume:96 Page:1898-1905
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Zhou Yuye¹²,Tan Congrui¹,Zenobi Renato¹^ORCID

Affiliation:

1. Department of Chemistry and Applied Biosciences, Swiss Federal Institute of Technology (ETH), CH-8093 Zürich, Switzerland

2. School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Chemistry, Division of Applied Physical Chemistry, Analytical Chemistry, KTH Royal Institute of Technology, SE-10044 Stockholm, Sweden

Funder

Vetenskapsr?det

Schweizerischer Nationalfonds zur F?rderung der Wissenschaftlichen Forschung

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.analchem.3c03930

Reference57 articles.

1. Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses

2. Site-specific glycan analysis of the SARS-CoV-2 spike

3. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein

4. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2

5. ACE2 and ACE: structure-based insights into mechanism, regulation and receptor recognition by SARS-CoV

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